Design of a stabilized He-Ne laser by using a thin-film heater.

Details concerning the design of the stabilization system for a He-Ne laser based on a two-mode method that uses a thin-film heater are discussed. The stability is evaluated by measuring the beat signal between two stabilized lasers; it is 1.1 × 10(-12), expressed in terms of the root Allan variance (τ = 35 s).

Two genes encode the two subunits of cottonseed catalase.

The isolation and sequence of a cDNA encoding a developmentally distinct subunit of cottonseed catalase are presented. A 1.8-kb cDNA was selected from a cDNA library constructed with poly(A)+ RNA isolated from 3-day-old dark-grown cotyledons in which a second subunit (designated SU 2 in an earlier publication) of catalase was predominantly synthesized. The cDNA encodes a 492-amino acid peptide with a calculated Mr of 56,900. The nucleotide sequence is 76% identical to a cDNA encoding another subunit (SU 1) which was predominantly synthesized in 1-day-old-cotyledons. Most of the divergence occurs in the 5' and 3' non-coding regions, and at the third positions of the codons. The deduced amino acid sequence is 92% identical to that of SU 1. Denaturing isoelectric focusing and SDS-PAGE of products transcribed and translated in vitro from these cDNAs revealed that the cDNA selected from the "1-day" library encoded SU 1 and the cDNA selected from the "3-day" library (this paper) encoded SU 2 of catalase. These data and results from Southern blot analyses of genomic DNA indicate that there are two genes encoding catalase subunits in cotton cotyledons, with only one copy of SU 1 and at least two copies of SU 2 in the genome. A peroxisomal targeting signal, e.g., Ser-Lys-Leu, is not located at the C-terminus of either subunit, or within 25 residues of the C-terminus of SU 1, although it occurs at six residues upstream from the C-terminus of SU 2. A possible location of a targeting sequence for catalase and other peroxisomal proteins lacking the C-terminal tripeptide motif is proposed.

Biogenesis of catalase in glyoxysomes and leaf-type peroxisomes of sunflower cotyledons.

Eight charge isoforms of catalase (EC 1.11.1.6.) appeared in the peroxisomes of sunflower cotyledons during growth after germination (2.5 days of dark, continuous light thereafter). In the light, when glyoxysomes were transformed to leaf-type peroxisomes, the five more-basic forms (CAT 1 through CAT 5) became more prominent, while amounts of the three more-acidic forms (CAT 6 through CAT 8) decreased considerably. The isoforms CAT 1 through CAT 5 were hybrids of 55- and 59-kDa subunits, whereas CAT 6 through CAT 8 contained 55-kDa subunits exclusively. The catalase translation products changed during the transition of glyoxysomes to leaf-type peroxisomes. Polyadenylated RNA from 2-day-old cotyledons directed synthesis of 56-kDa subunits, whereas 59-kDa subunits predominated after in vitro translation of RNA from 4-day-old cotyledons. Both translation products were processed to lower molecular weight forms in vivo. The 56-kDa translation products were precursors for 55-kDa subunits in glyoxysomes. It could not be decided however, whether the 59-kDa precursors were processed to 56-kDa or 55-kDa subunits, because both subunits of lower molecular weight were present in leaf-type peroxisomes. Some of the 59-kDa precursors escaped proteolytic processing and formed hybrid isoforms (CAT 1 through CAT 5) with mature 55-kDa subunits. This type of isoform formation, i.e., condensation of mature and unprocessed subunits, has not yet been described for other plant catalases. In summary, the results showed that the postgerminative changes in the number and abundance of catalase isoforms resulted from changes in translation (transcription) of catalase precursors and assembly of proteolytically processed and unprocessed subunits into tetramers within peroxisomes acquiring leaf peroxisomal function.